PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity |
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Authors: | Badrick Alison C Hamilton Amanda J Bernhardt Paul V Jones Christopher E Kappler Ulrike Jennings Michael P McEwan Alastair G |
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Affiliation: | Centre for Metals in Biology, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia. |
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Abstract: | PrrC is a Sco homologue in Rhodobacter sphaeroides that is associated with PrrBA, a two-component signal transduction system that induces photosynthesis gene expression in response to a decrease in oxygen tension. Although Sco proteins have been shown to bind copper the observation that they are structurally-related to thioredoxins suggested that they might possess thiol-disulfide oxidoreductase activity. Our results show that PrrC reduces Cu(2+) to Cu(+) and possesses disulfide reductase activity. These results indicate that some bacterial Sco proteins may have biochemical properties that are distinct from those of mitochondrial Sco proteins. |
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Keywords: | BC, bathocuproine 2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline BSA, bovine serum albumin Co(trans-diammac), trans-6,13-dimethyl-(1,4,8,11-tetraazacyclotetradecane-6,13-diamine)cobalt(III) perchlorate cPrrC, cleaved PrrC DTNB, 5,5-dithiobis(2-nitrobenzoic acid) DTT, dithiothreitol, (2R,3R)-1,4-bis-sulfanylbutane-2,3-diol EPR, Electron Paramagnetic Resonance htPrrC, 6×-his-tagged PrrC IPTG, isopropyl-β- smallcaps" >d-thiogalactopyranoside oxPrrC, oxidised PrrC PrrC, photosynthetic regulatory response rPrrC, reduced PrrC Sco, synthesis of cytochrome oxidase Trx, thioredoxin |
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